Action of glucoamylase from Aspergillus niger on phosphorylated substrate.
Glucoamylase (1,4-alpha-D-glucan glucohydrolase, EC 3.2.1.3) from Aspergillus niger was purified to be free from alpha-amylase and phosphatase (glucose 6-phosphate as substrate). The phosphatase was well separated from the glucoamylase by phosphocellulose ion-exchange chromatography. The glucoamylase action was prevented by the esterified phosphate groups of the substrate. Thus, the extensive action of the glucoamylase on potato starch exposed the 6-posphorylglucosyl residue of the starch at the non-reducing terminal and large molecular weight limit dextrins remained. The concomitant action of the phosphatase was necessary for the complete degradation of the starch.
D000818:Animals; D001234:Aspergillus niger / Q000201:enzymology*; D002852:Chromatography, Ion Exchange; D005087:Glucan 1,4-alpha-Glucosidase / Q000378:metabolism*; D005959:Glucosidases / Q000378:metabolism*; D006868:Hydrolysis; D008112:Liver Glycogen / Q000378:metabolism; D010766:Phosphorylation
D008112:Liver Glycogen; D005959:Glucosidases; D005087:Glucan 1,4-alpha-Glucosidase